Mediator of RNA polymerase II transcription subunit 1

Details

Name
Mediator of RNA polymerase II transcription subunit 1
Kind
protein
Synonyms
  • Activator-recruited cofactor 205 kDa component
  • ARC205
  • CRSP1
  • CRSP200
  • DRIP205
  • DRIP230
  • Mediator complex subunit 1
  • p53 regulatory protein RB18A
  • PBP
  • Peroxisome proliferator-activated receptor-binding protein
  • PPAR-binding protein
  • PPARBP
  • PPARGBP
  • RB18A
  • Thyroid hormone receptor-associated protein complex 220 kDa component
  • Thyroid receptor-interacting protein 2
  • TR-interacting protein 2
  • TRAP220
  • TRIP-2
  • TRIP2
  • Vitamin D receptor-interacting protein complex component DRIP205
Gene Name
MED1
UniProtKB Entry
Q15648Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0008320|Mediator of RNA polymerase II transcription subunit 1
MKAQGETEESEKLSKMSSLLERLHAKFNQNRPWSETIKLVRQVMEKRVVMSSGGHQHLVS
CLETLQKALKVTSLPAMTDRLESIARQNGLGSHLSASGTECYITSDMFYVEVQLDPAGQL
CDVKVAHHGENPVSCPELVQQLREKNFDEFSKHLKGLVNLYNLPGDNKLKTKMYLALQSL
EQDLSKMAIMYWKATNAGPLDKILHGSVGYLTPRSGGHLMNLKYYVSPSDLLDDKTASPI
ILHENNVSRSLGMNASVTIEGTSAVYKLPIAPLIMGSHPVDNKWTPSFSSITSANSVDLP
ACFFLKFPQPIPVSRAFVQKLQNCTGIPLFETQPTYAPLYELITQFELSKDPDPIPLNHN
MRFYAALPGQQHCYFLNKDAPLPDGRSLQGTLVSKITFQHPGRVPLILNLIRHQVAYNTL
IGSCVKRTILKEDSPGLLQFEVCPLSESRFSVSFQHPVNDSLVCVVMDVQDSTHVSCKLY
KGLSDALICTDDFIAKVVQRCMSIPVTMRAIRRKAETIQADTPALSLIAETVEDMVKKNL
PPASSPGYGMTTGNNPMSGTTTPTNTFPGGPITTLFNMSMSIKDRHESVGHGEDFSKVSQ
NPILTSLLQITGNGGSTIGSSPTPPHHTPPPVSSMAGNTKNHPMLMNLLKDNPAQDFSTL
YGSSPLERQNSSSGSPRMEICSGSNKTKKKKSSRLPPEKPKHQTEDDFQRELFSMDVDSQ
NPIFDVNMTADTLDTPHITPAPSQCSTPPTTYPQPVPHPQPSIQRMVRLSSSDSIGPDVT
DILSDIAEEASKLPSTSDDCPAIGTPLRDSSSSGHSQSTLFDSDVFQTNNNENPYTDPAD
LIADAAGSPSSDSPTNHFFHDGVDFNPDLLNSQSQSGFGEEYFDESSQSGDNDDFKGFAS
QALNTLGVPMLGGDNGETKFKGNNQADTVDFSIISVAGKALAPADLMEHHSGSQGPLLTT
GDLGKEKTQKRVKEGNGTSNSTLSGPGLDSKPGKRSRTPSNDGKSKDKPPKRKKADTEGK
SPSHSSSNRPFTPPTSTGGSKSPGSAGRSQTPPGVATPPIPKITIQIPKGTVMVGKPSSH
SQYTSSGSVSSSGSKSHHSHSSSSSSSASTSGKMKSSKSEGSSSSKLSSSMYSSQGSSGS
SQSKNSSQSGGKPGSSPITKHGLSSGSSSTKMKPQGKPSSLMNPSLSKPNISPSHSRPPG
GSDKLASPMKPVPGTPPSSKAKSPISSGSGGSHMSGTSSSSGMKSSSGLGSSGSLSQKTP
PSSNSCTASSSSFSSSGSSMSSSQNQHGSSKGKSPSRNKKPSLTAVIDKLKHGVVTSGPG
GEDPLDGQMGVSTNSSSHPMSSKHNMSGGEFQGKREKSDKDKSKVSTSGSSVDSSKKTSE
SKNVGSTGVAKIIISKHDGGSPSIKAKVTLQKPGESSGEGLRPQMASSKNYGSPLISGST
PKHERGSPSHSKSPAYTPQNLDSESESGSSIAEKSYQNSPSSDDGIRPLPEYSTEKHKKH
KKEKKKVKDKDRDRDRDKDRDKKKSHSIKPESWSKSPISSDQSLSMTSNTILSADRPSRL
SPDFMIGEEDDDLMDVALIGN
Number of residues
1581
Molecular Weight
168476.57
Theoretical pI
9.1
GO Classification
Functions
DNA-binding transcription factor binding / general transcription initiation factor binding / histone acetyltransferase binding / nuclear estrogen receptor binding / nuclear receptor binding / nuclear receptor coactivator activity / nuclear retinoic acid receptor binding / nuclear thyroid hormone receptor binding / nuclear vitamin D receptor binding / promoter-specific chromatin binding / RNA polymerase II cis-regulatory region sequence-specific DNA binding / transcription coactivator binding / transcription coregulator activity / transcription corepressor activity
Processes
animal organ regeneration / G0 to G1 transition / hematopoietic stem cell differentiation / mRNA transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / nuclear receptor-mediated steroid hormone signaling pathway / positive regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / positive regulation of transcription elongation by RNA polymerase II / positive regulation of transcription initiation by RNA polymerase II / positive regulation of type II interferon-mediated signaling pathway / protein import into nucleus / protein ubiquitination / regulation of transcription by RNA polymerase II / RNA polymerase II preinitiation complex assembly / thyroid hormone receptor signaling pathway
Components
core mediator complex
General Function
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781)
Specific Function
chromatin binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Nucleus
Gene sequence
>lcl|BSEQ0013052|Mediator of RNA polymerase II transcription subunit 1 (MED1)
ATGAAAGCTCAGGGGGAAACCGAGGAGTCAGAAAAGCTGAGTAAGATGAGTTCTCTCCTG
GAACGGCTCCATGCAAAATTTAACCAAAATAGACCCTGGAGTGAAACCATTAAGCTTGTG
CGTCAAGTCATGGAGAAGAGGGTTGTGATGAGTTCTGGAGGGCATCAACATTTGGTCAGC
TGTTTGGAGACATTGCAGAAGGCTCTCAAAGTAACATCTTTACCAGCAATGACTGATCGT
TTGGAGTCCATAGCAAGACAGAATGGACTGGGCTCTCATCTCAGTGCCAGTGGCACTGAA
TGTTACATCACGTCAGATATGTTCTATGTGGAAGTGCAGTTAGATCCTGCAGGACAGCTT
TGTGATGTAAAAGTGGCTCACCATGGGGAGAATCCTGTGAGCTGTCCGGAGCTTGTACAG
CAGCTAAGGGAAAAAAATTTTGATGAATTTTCTAAGCACCTTAAGGGCCTTGTTAATCTG
TATAACCTTCCAGGGGACAACAAACTGAAGACTAAAATGTACTTGGCTCTCCAATCCTTA
GAACAAGATCTTTCTAAAATGGCAATTATGTACTGGAAAGCAACTAATGCTGGTCCCTTG
GATAAGATTCTTCATGGAAGTGTTGGCTATCTCACACCAAGGAGTGGGGGTCATTTAATG
AACCTGAAGTACTATGTCTCTCCTTCTGACCTACTGGATGACAAGACTGCATCTCCCATC
ATTTTGCATGAGAATAATGTTTCTCGATCTTTGGGCATGAATGCATCAGTGACAATTGAA
GGAACATCTGCTGTGTACAAACTCCCAATTGCACCATTAATTATGGGGTCACATCCAGTT
GACAATAAATGGACCCCTTCCTTCTCCTCAATCACCAGTGCCAACAGTGTTGATCTTCCT
GCCTGTTTCTTCTTGAAATTTCCCCAGCCAATCCCAGTATCTAGAGCATTTGTTCAGAAA
CTGCAGAACTGCACAGGAATTCCATTGTTTGAAACTCAACCAACTTATGCACCCCTGTAT
GAACTGATCACTCAGTTTGAGCTATCAAAGGACCCTGACCCCATACCTTTGAATCACAAC
ATGAGATTTTATGCTGCTCTTCCTGGTCAGCAGCACTGCTATTTCCTCAACAAGGATGCT
CCTCTTCCAGATGGCCGAAGTCTACAGGGAACCCTTGTTAGCAAAATCACCTTTCAGCAC
CCTGGCCGAGTTCCTCTTATCCTAAATCTGATCAGACACCAAGTGGCCTATAACACCCTC
ATTGGAAGCTGTGTCAAAAGAACTATTCTGAAAGAAGATTCTCCTGGGCTTCTCCAATTT
GAAGTGTGTCCTCTCTCAGAGTCTCGTTTCAGCGTATCTTTTCAGCACCCTGTGAATGAC
TCCCTGGTGTGTGTGGTAATGGATGTGCAGGACTCAACACATGTGAGCTGTAAACTCTAC
AAAGGGCTGTCGGATGCACTGATCTGCACAGATGACTTCATTGCCAAAGTTGTTCAAAGA
TGTATGTCCATCCCTGTGACGATGAGGGCTATTCGGAGGAAAGCTGAAACCATTCAAGCC
GACACCCCAGCACTGTCCCTCATTGCAGAGACAGTTGAAGACATGGTGAAAAAGAACCTG
CCCCCGGCTAGCAGCCCAGGGTATGGCATGACCACAGGCAACAACCCAATGAGTGGTACC
ACTACACCAACCAACACCTTTCCGGGGGGTCCCATTACCACCTTGTTTAATATGAGCATG
AGCATCAAAGATCGGCATGAGTCGGTGGGCCATGGGGAGGACTTCAGCAAGGTGTCTCAG
AACCCAATTCTTACCAGTTTGTTGCAAATCACAGGGAACGGGGGGTCTACCATTGGCTCG
AGTCCGACCCCTCCTCATCACACGCCGCCACCTGTCTCTTCGATGGCCGGCAACACCAAG
AACCACCCGATGCTCATGAACCTTCTTAAAGATAATCCTGCCCAGGATTTCTCAACCCTT
TATGGAAGCAGCCCTTTAGAAAGGCAGAACTCCTCTTCCGGCTCACCCCGCATGGAAATA
TGCTCGGGGAGCAACAAGACCAAGAAAAAGAAGTCATCAAGATTACCACCTGAGAAACCA
AAGCACCAGACTGAAGATGACTTTCAGAGGGAGCTATTTTCAATGGATGTTGACTCACAG
AACCCTATCTTTGATGTCAACATGACAGCTGACACGCTGGATACGCCACACATCACTCCA
GCTCCAAGCCAGTGTAGCACTCCCCCAACAACTTACCCACAACCAGTACCTCACCCCCAA
CCCAGTATTCAAAGGATGGTCCGACTATCCAGTTCAGACAGCATTGGCCCAGATGTAACT
GACATCCTTTCAGACATTGCAGAAGAAGCTTCTAAACTTCCCAGCACTAGTGATGATTGC
CCAGCCATTGGCACCCCTCTTCGAGATTCTTCAAGCTCTGGGCATTCTCAGAGTACCCTG
TTTGACTCTGATGTCTTTCAAACTAACAATAATGAAAATCCATACACTGATCCAGCTGAT
CTTATTGCAGATGCTGCTGGAAGCCCCAGTAGTGACTCTCCTACCAATCATTTTTTTCAT
GATGGAGTAGATTTCAATCCTGATTTATTGAACAGCCAGAGCCAAAGTGGTTTTGGAGAA
GAATATTTTGATGAAAGCAGCCAAAGTGGGGATAATGATGATTTCAAAGGATTTGCATCT
CAGGCACTAAATACTTTGGGGGTGCCAATGCTTGGAGGTGATAATGGGGAGACCAAGTTT
AAGGGCAATAACCAAGCCGACACAGTTGATTTCAGTATTATTTCAGTAGCCGGCAAAGCT
TTAGCTCCTGCAGATCTTATGGAGCATCACAGTGGTAGTCAGGGTCCTTTACTGACCACT
GGGGACTTAGGGAAAGAAAAGACTCAAAAGAGGGTAAAGGAAGGCAATGGCACCAGTAAT
AGTACTCTCTCGGGGCCCGGATTAGACAGCAAACCAGGGAAGCGCAGTCGGACCCCTTCT
AATGATGGGAAAAGCAAAGATAAGCCTCCAAAGCGGAAGAAGGCAGACACTGAGGGAAAG
TCTCCATCTCATAGTTCTTCTAACAGACCTTTTACCCCACCTACCAGTACAGGTGGATCT
AAATCGCCAGGCAGTGCAGGAAGATCTCAGACTCCCCCAGGTGTTGCCACACCACCCATT
CCCAAAATCACTATTCAGATTCCTAAGGGAACAGTGATGGTGGGCAAGCCTTCCTCTCAC
AGTCAGTATACCAGCAGTGGTTCTGTGTCTTCCTCAGGCAGCAAAAGCCACCATAGCCAT
TCTTCCTCCTCTTCCTCATCTGCTTCCACCTCAGGGAAGATGAAAAGCAGTAAATCAGAA
GGTTCATCAAGTTCCAAGTTAAGTAGCAGTATGTATTCTAGCCAGGGGTCTTCTGGATCT
AGCCAGTCCAAAAATTCATCCCAGTCTGGGGGGAAGCCAGGCTCCTCTCCCATAACCAAG
CATGGACTGAGCAGTGGCTCTAGCAGCACCAAGATGAAACCTCAAGGAAAGCCATCATCA
CTTATGAATCCTTCTTTAAGTAAACCAAACATATCCCCTTCTCATTCAAGGCCACCTGGA
GGCTCTGACAAGCTTGCCTCTCCAATGAAGCCTGTTCCTGGAACTCCTCCATCCTCTAAA
GCCAAGTCCCCTATCAGTTCAGGTTCTGGTGGTTCTCATATGTCTGGAACTAGTTCAAGC
TCTGGCATGAAGTCATCTTCAGGGTTAGGATCCTCAGGCTCGTTGTCCCAGAAAACTCCC
CCATCATCTAATTCCTGTACGGCATCTTCCTCCTCCTTTTCCTCAAGTGGCTCTTCCATG
TCATCCTCTCAGAACCAGCATGGGAGTTCTAAAGGAAAATCTCCCAGCAGAAACAAGAAG
CCGTCCTTGACAGCTGTCATAGATAAACTGAAGCATGGGGTTGTCACCAGTGGCCCTGGG
GGTGAAGACCCACTGGACGGCCAGATGGGGGTGAGCACAAATTCTTCCAGCCATCCTATG
TCCTCCAAACATAACATGTCAGGAGGAGAGTTTCAGGGCAAGCGTGAGAAAAGTGATAAA
GACAAATCAAAGGTTTCCACCTCCGGGAGTTCAGTGGATTCTTCTAAGAAGACCTCAGAG
TCAAAAAATGTGGGGAGCACAGGTGTGGCAAAAATTATCATCAGTAAGCATGATGGAGGC
TCCCCTAGCATTAAAGCCAAAGTGACTTTGCAGAAACCTGGGGAAAGTAGTGGAGAAGGG
CTTAGGCCTCAAATGGCTTCTTCTAAAAACTATGGCTCTCCACTCATCAGTGGTTCCACT
CCAAAGCATGAGCGTGGCTCTCCCAGCCATAGTAAGTCACCAGCATATACCCCCCAGAAT
CTGGACAGTGAAAGTGAGTCAGGCTCCTCCATAGCAGAGAAATCTTATCAGAATAGTCCC
AGCTCAGACGATGGTATCCGACCACTTCCAGAATACAGCACAGAGAAACATAAGAAGCAC
AAAAAGGAAAAGAAGAAAGTAAAAGACAAAGATAGGGACCGAGACCGGGACAAAGACCGA
GACAAGAAAAAATCTCATAGCATCAAGCCAGAGAGTTGGTCCAAATCACCCATCTCTTCA
GACCAGTCCTTGTCTATGACAAGTAACACAATCTTATCTGCAGACAGACCCTCAAGGCTC
AGCCCAGACTTTATGATTGGGGAGGAAGATGATGATCTTATGGATGTGGCCCTGATTGGG
AATTAG
Chromosome Location
17
Locus
17q12
External Identifiers
ResourceLink
UniProtKB IDQ15648
UniProtKB Entry NameMED1_HUMAN
GenBank Protein ID2765322
GenBank Gene IDY13467
GeneCard IDMED1
HGNC IDHGNC:9234
PDB ID(s)1RJK, 1RK3, 1RKG, 1RKH, 2O4J, 2O4R, 2ZFX, 3A2H, 3AUN, 3VJS, 3VJT, 3VRT, 3VRU, 3VRV, 3VRW, 3W0G, 3W0H, 3W0I, 3W0J, 3W5P, 3W5Q, 3W5R, 3W5T, 3WT5, 3WT6, 3WT7, 3WTQ, 4YNK, 5AWJ, 5AWK, 5B41, 5B5B, 5GIC, 5GID, 5GIE, 5XPM, 5XPN, 5XPO, 5XPP, 5XUQ, 5XZF, 5XZH, 5ZWE, 5ZWF, 5ZWH, 5ZWI, 6D94, 6JEZ, 6K5O, 6ONJ, 7C7V, 7C7W, 7EMF, 7ENA, 7ENC, 7ENJ, 7OXU, 7VQP, 8GXQ, 8GXS
KEGG IDhsa:5469
NCBI Gene ID5469
General References
  1. Drane P, Barel M, Balbo M, Frade R: Identification of RB18A, a 205 kDa new p53 regulatory protein which shares antigenic and functional properties with p53. Oncogene. 1997 Dec 18;15(25):3013-24. [Article]
  2. Yuan CX, Ito M, Fondell JD, Fu ZY, Roeder RG: The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion. Proc Natl Acad Sci U S A. 1998 Jul 7;95(14):7939-44. [Article]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Naar AM, Beaurang PA, Zhou S, Abraham S, Solomon W, Tjian R: Composite co-activator ARC mediates chromatin-directed transcriptional activation. Nature. 1999 Apr 29;398(6730):828-32. [Article]
  5. Rachez C, Gamble M, Chang CP, Atkins GB, Lazar MA, Freedman LP: The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes. Mol Cell Biol. 2000 Apr;20(8):2718-26. [Article]
  6. Rachez C, Lemon BD, Suldan Z, Bromleigh V, Gamble M, Naar AM, Erdjument-Bromage H, Tempst P, Freedman LP: Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex. Nature. 1999 Apr 29;398(6730):824-8. [Article]
  7. Lee JW, Choi HS, Gyuris J, Brent R, Moore DD: Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Mol Endocrinol. 1995 Feb;9(2):243-54. [Article]
  8. Gu W, Malik S, Ito M, Yuan CX, Fondell JD, Zhang X, Martinez E, Qin J, Roeder RG: A novel human SRB/MED-containing cofactor complex, SMCC, involved in transcription regulation. Mol Cell. 1999 Jan;3(1):97-108. [Article]
  9. Zhang J, Fondell JD: Identification of mouse TRAP100: a transcriptional coregulatory factor for thyroid hormone and vitamin D receptors. Mol Endocrinol. 1999 Jul;13(7):1130-40. [Article]
  10. Atkins GB, Hu X, Guenther MG, Rachez C, Freedman LP, Lazar MA: Coactivators for the orphan nuclear receptor RORalpha. Mol Endocrinol. 1999 Sep;13(9):1550-7. [Article]
  11. Burakov D, Wong CW, Rachez C, Cheskis BJ, Freedman LP: Functional interactions between the estrogen receptor and DRIP205, a subunit of the heteromeric DRIP coactivator complex. J Biol Chem. 2000 Jul 7;275(27):20928-34. [Article]
  12. Warnmark A, Almlof T, Leers J, Gustafsson JA, Treuter E: Differential recruitment of the mammalian mediator subunit TRAP220 by estrogen receptors ERalpha and ERbeta. J Biol Chem. 2001 Jun 29;276(26):23397-404. Epub 2001 Apr 12. [Article]
  13. Wang Q, Sharma D, Ren Y, Fondell JD: A coregulatory role for the TRAP-mediator complex in androgen receptor-mediated gene expression. J Biol Chem. 2002 Nov 8;277(45):42852-8. Epub 2002 Sep 5. [Article]
  14. Ge K, Guermah M, Yuan CX, Ito M, Wallberg AE, Spiegelman BM, Roeder RG: Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated adipogenesis. Nature. 2002 May 30;417(6888):563-7. [Article]
  15. Kang YK, Guermah M, Yuan CX, Roeder RG: The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2642-7. Epub 2002 Feb 26. [Article]
  16. Sharma D, Fondell JD: Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormone-responsive promoters in vivo. Proc Natl Acad Sci U S A. 2002 Jun 11;99(12):7934-9. Epub 2002 May 28. [Article]
  17. Coulthard VH, Matsuda S, Heery DM: An extended LXXLL motif sequence determines the nuclear receptor binding specificity of TRAP220. J Biol Chem. 2003 Mar 28;278(13):10942-51. Epub 2003 Jan 29. [Article]
  18. Wallberg AE, Yamamura S, Malik S, Spiegelman BM, Roeder RG: Coordination of p300-mediated chromatin remodeling and TRAP/mediator function through coactivator PGC-1alpha. Mol Cell. 2003 Nov;12(5):1137-49. [Article]
  19. Wu Q, Burghardt R, Safe S: Vitamin D-interacting protein 205 (DRIP205) coactivation of estrogen receptor alpha (ERalpha) involves multiple domains of both proteins. J Biol Chem. 2004 Dec 17;279(51):53602-12. Epub 2004 Oct 5. [Article]
  20. Sato S, Tomomori-Sato C, Parmely TJ, Florens L, Zybailov B, Swanson SK, Banks CA, Jin J, Cai Y, Washburn MP, Conaway JW, Conaway RC: A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology. Mol Cell. 2004 Jun 4;14(5):685-91. [Article]
  21. Malik S, Guermah M, Yuan CX, Wu W, Yamamura S, Roeder RG: Structural and functional organization of TRAP220, the TRAP/mediator subunit that is targeted by nuclear receptors. Mol Cell Biol. 2004 Sep;24(18):8244-54. [Article]
  22. Zhang X, Krutchinsky A, Fukuda A, Chen W, Yamamura S, Chait BT, Roeder RG: MED1/TRAP220 exists predominantly in a TRAP/ Mediator subpopulation enriched in RNA polymerase II and is required for ER-mediated transcription. Mol Cell. 2005 Jul 1;19(1):89-100. [Article]
  23. Pandey PK, Udayakumar TS, Lin X, Sharma D, Shapiro PS, Fondell JD: Activation of TRAP/mediator subunit TRAP220/Med1 is regulated by mitogen-activated protein kinase-dependent phosphorylation. Mol Cell Biol. 2005 Dec;25(24):10695-710. [Article]
  24. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [Article]
  25. Udayakumar TS, Belakavadi M, Choi KH, Pandey PK, Fondell JD: Regulation of Aurora-A kinase gene expression via GABP recruitment of TRAP220/MED1. J Biol Chem. 2006 May 26;281(21):14691-9. Epub 2006 Mar 30. [Article]
  26. Zhou H, Kim S, Ishii S, Boyer TG: Mediator modulates Gli3-dependent Sonic hedgehog signaling. Mol Cell Biol. 2006 Dec;26(23):8667-82. Epub 2006 Sep 25. [Article]
  27. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [Article]
  28. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [Article]
  29. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [Article]
  30. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [Article]
  31. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
  32. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [Article]
  33. Cho Y, Noshiro M, Choi M, Morita K, Kawamoto T, Fujimoto K, Kato Y, Makishima M: The basic helix-loop-helix proteins differentiated embryo chondrocyte (DEC) 1 and DEC2 function as corepressors of retinoid X receptors. Mol Pharmacol. 2009 Dec;76(6):1360-9. doi: 10.1124/mol.109.057000. Epub 2009 Sep 28. [Article]
  34. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [Article]
  35. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [Article]
  36. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
  37. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  38. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [Article]
  39. Mizuta S, Minami T, Fujita H, Kaminaga C, Matsui K, Ishino R, Fujita A, Oda K, Kawai A, Hasegawa N, Urahama N, Roeder RG, Ito M: CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel pathway for GATA1 function. Genes Cells. 2014 Jan;19(1):28-51. doi: 10.1111/gtc.12104. Epub 2013 Nov 19. [Article]
  40. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
BecocalcidiolinvestigationalunknowntargetDetails